PURIFICATION AND CHARACTERIZATION OF 2 ODORANT-BINDING PROTEINS FROM NASAL TISSUE OF RABBIT AND PIG

被引：77

作者：

Dal Monte, M

ANDREINI, I

REVOLTELLA, R

PELOSI, P

机构：

[1] UNIV PISA, IST IND AGR,VIA S MICHELE 4, I-56100 PISA, ITALY

[2] CNR, IST MUTAGENESI & DIFFERENZIAMENTO, I-56100 PISA, ITALY

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1991年 / 99卷 / 02期

关键词：

D O I：

10.1016/0305-0491(91)90068-O

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. Soluble proteins showing binding activity to 2-isobutyl-3-methoxypyrazine have been purified to homogeneity from rabbit and pig nasal tissue; their characteristics are similar to the bovine odorant-binding protein and are to be considered members of the same family. 2. The rabbit protein is a homodimer with subunits of M(r) 19k and an isoelectric point of 4.7, whereas the pig protein appears to consist of a single polypeptide chain of M(r) 22k and an isoelectric point of 4.2. 3. Both proteins bind 2-isobutyl-3-methoxypyrazine with dissociation constants in the micromolar range. 4. Antibodies against the bovine OBP react well with the rabbit protein, and slightly with the porcine one.

引用

页码：445 / 451

页数：7

共 19 条

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